LAIR-1 Background Information Leukocyte-associated Ig-like receptor-1, known as LAIR-1, is a transmembrane glycoprotein that is constitutively expressed on the majority of human peripheral blood mononuclear leukocytes. LAIR-1 is phosphorylated at the Tyr-233 and Tyr-263 residues, and once activated, LAIR-1 recruits SHP-1, an SH2 domain-containing phosphatase (3-5). SHP-1 is highly expressed in hematopoietic cells and functions as a negative regulator of cell signaling. SHP-1 also contributes to the establishment of TCR signaling thresholds in both developing and mature T lymphocytes (4). The binding of LAIR-1 to SHP-1 functions as a mechanism of regulating the role of SHP-1 in cell signaling. Occupancy of LAIR-1 on human myelomonocytic leukemic cell lines inhibits proliferation and leads to programmed cell death (PCD), and cross-linking of the LAIR-1 antigen on natural killer (NK) cells results in strong inhibition of NK cell-mediated cytotoxity. Protein kinases responsible for tyrosine phosphorylation of LAIR-1 may belong to the Src family since PP1, a Src family kinase inhibitor, significantly inhibits its phosphorylation.
LAIR-1 (N-21)
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LAIR-1 (N-21): sc-21569. Western blot analysis of LAIR-1 expression in HuT 78 whole cell lysate.
LAIR-1 (N-21): sc-21569. Western blot analysis of LAIR-1 expression in non-transfected: sc-117752 (A) and human LAIR-1 transfected: sc-114216 (B) 293T whole cell lysates.
